The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase-Reference-Cited by-同舟云学术

The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase

Published:1996-04 Issue:4 Volume:3 Page:340-345
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Grzesiek Stephan,Bax Ad,Clore G. Marius,Gronenborn Angela M.,Hu Jin-Shan,Kaufman Joshua,Palmer Ira,Stahl Stephen J.,Wingfield Paul T

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsb0496-340.pdf

Reference34 articles.

1. Analysis of human immunodeficiency virus type 1 nef gene sequences present in vivo

2. Importance of the nef gene for maintenance of high virus loads and for development of AIDS

3. Absence of Intact nef Sequences in a Long-Term Survivor with Nonprogressive HIV-1 Infection

4. Genomic Structure of an Attenuated Quasi Species of HIV-1 from a Blood Transfusion Donor and Recipients

5. Protective Effects of a Live Attenuated SIV Vaccine with a Deletion in the nef Gene

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